RESUMO
Epidermal growth factor receptor (EGFR) plays an important role in cell proliferation at non-small cell lung cancer (NSCLC). Therefore, targeted therapy of cancer via this kind of receptor is highly interested. Small molecule drugs such as erlotinib and gefitinib inhibit EGFR tyrosine kinase and thus suppress cell proliferation. At this paper, erlotinib interaction with EGFR on the cell surface was studied via surface plasmon resonance (SPR) and molecular docking methods. Kinetic parameters indicated that erlotinib affinity toward EGFR was increased through increment of temperature. The thermodynamic analysis showed that van der Waals and hydrogen binding forces play a major role in the interaction of erlotinib with EGFR. Docking results showed that Domain II in EGFR has role in the interaction with erlotinib. Besides, the binding energy for this interaction was -10.7 kcal/mol, which is suitable for binding of erlotinib to Domain II in EGFR.